Novel aspects of the electrophysiology of mitochondrial porin.
The recent findings that mitochondrial porin, VDAC, participates in supramolecular complexes and is present in the plasmamembrane need to be reconciled with its biophysical properties. We report here that VDAC often displays previously unobserved or unappreciated behaviors. Reconstituted VDAC can: a) exhibit fast gating when in any of many conductance substates; b) close completely, although briefly, on its own; c) close for a long periods, in the presence of König's polyanion; d) take several milliseconds to re-open when an applied transmembrane potential is switched off; e) be desensitized by prolonged exposure to high voltages, so that it will not re-open to the full conductance state upon subsequent return to zero voltage; f) display polarity-dependent voltage-induced closure. These behaviors are especially noticeable when the observations are conducted on a single reincorporated channel, suggesting that interactions between copies of VDAC may play a role in determining its electrophysiological properties. Any model of VDAC's structure, gating and function should take these observations into account.
Báthori
G
G
CNR Unit for Biomembranes, Department of Biomedical Sciences, University of Padova, Italy.
Szabó
I
I
Schmehl
I
I
Tombola
F
F
Messina
A
A
De Pinto
V
V
Zoratti
M
M
D000818:Animals; D002417:Cattle; D004594:Electrophysiology; D066298:In Vitro Techniques; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry / Q000502:physiology; D007700:Kinetics; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D008929:Mitochondria, Heart / Q000502:physiology; D008930:Mitochondria, Liver / Q000502:physiology; D008954:Models, Biological; D018272:Porins; D051381:Rats; D050994:Voltage-Dependent Anion Channels
D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D050994:Voltage-Dependent Anion Channels